ID   M21_STRPY               Reviewed;         407 AA.
AC   P50468;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=M protein, serotype 2.1;
DE   Flags: Precursor;
GN   Name=emmL2.1;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T2/44/RB4/119;
RX   PubMed=1370269; DOI=10.1128/iai.60.1.124-135.1992;
RA   Bessen D.E., Fischetti V.A.;
RT   "Nucleotide sequences of two adjacent M or M-like protein genes of group A
RT   streptococci: different RNA transcript levels and identification of a
RT   unique immunoglobulin A-binding protein.";
RL   Infect. Immun. 60:124-135(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-305.
RC   STRAIN=T2/44/RB4;
RX   PubMed=2258705; DOI=10.1084/jem.172.6.1757;
RA   Bessen D.E., Fischetti V.A.;
RT   "Differentiation between two biologically distinct classes of group A
RT   streptococci by limited substitutions of amino acids within the shared
RT   region of M protein-like molecules.";
RL   J. Exp. Med. 172:1757-1764(1990).
CC   -!- FUNCTION: This protein is one of the different antigenic serotypes of
CC       protein M. Protein M is closely associated with virulence of the
CC       bacterium and can render the organism resistant to phagocytosis.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- SIMILARITY: Belongs to the M protein family. {ECO:0000305}.
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DR   EMBL; X61276; CAA43581.1; -; Genomic_DNA.
DR   EMBL; X56398; CAA39808.1; -; Genomic_DNA.
DR   PIR; PH0139; PH0139.
DR   PIR; S23325; S23325.
DR   PDB; 5HYU; X-ray; 2.56 A; A=42-142.
DR   PDB; 5I0Q; X-ray; 2.29 A; A=42-141.
DR   PDBsum; 5HYU; -.
DR   PDBsum; 5I0Q; -.
DR   AlphaFoldDB; P50468; -.
DR   SMR; P50468; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR019950; M_anchor.
DR   InterPro; IPR003345; M_repeat.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF02370; M; 4.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   PRINTS; PR00015; GPOSANCHOR.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Coiled coil; Peptidoglycan-anchor; Phagocytosis;
KW   Repeat; Secreted; Signal; Virulence.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..377
FT                   /note="M protein, serotype 2.1"
FT                   /id="PRO_0000005611"
FT   PROPEP          378..407
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005612"
FT   REPEAT          62..80
FT                   /note="M 1"
FT   REPEAT          81..87
FT                   /note="1"
FT   REPEAT          88..94
FT                   /note="2"
FT   REPEAT          176..196
FT                   /note="M 2"
FT   REPEAT          211..231
FT                   /note="M 3"
FT   REPEAT          246..266
FT                   /note="M 4"
FT   REPEAT          281..301
FT                   /note="M 5"
FT   REGION          81..94
FT                   /note="2 X 7 AA tandem repeats"
FT   REGION          83..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           374..378
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        83..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         377
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   HELIX           60..84
FT                   /evidence="ECO:0007829|PDB:5I0Q"
SQ   SEQUENCE   407 AA;  46466 MW;  33CA053B7DB3C1EA CRC64;
     MARKDTNKQY SLRKLKTGTA SVAVAVAVLG AGFANQTTVK ANSKNPVPVK KEAKLSEAEL
     HDKIKNLEEE KAELFEKLDK VEEEHKKVEE EHKKDHEKLE KKSEDVERHY LRQLDQEYKE
     QQERQKNLEE LERQSQREVE KRYQEQLQKQ QQLEKEKQIS EASRKSLRRD LEASRAAKKD
     LEAEHQKLKE EKQISEASRK SLRRDLEASR AAKKDLEAEH QKLKEEKQIS EASRQGLSRD
     LEASRAAKKD LEAEHQKLKE EKQISEASRQ GLSRDLEASR EAKKKVEADL AEANSKLQAL
     EKLNKELEEG KKLSEKEKAE LQAKLEAEAK ALKEQLAKQA EELAKLKGNQ TPNAKVAPQA
     NRSRSAMTQQ KRTLPSTGET ANPFFTAAAA TVMVSAGMLA LKRKEEN